Sodium in PDB 7b3n: Amip Amidase-3 From Thermus Parvatiensis
Protein crystallography data
The structure of Amip Amidase-3 From Thermus Parvatiensis, PDB code: 7b3n
was solved by
S.Freitag-Pohl,
E.Pohl,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
43.68 /
1.79
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
64.539,
97.988,
148.723,
90,
90,
90
|
R / Rfree (%)
|
18.5 /
22.5
|
Other elements in 7b3n:
The structure of Amip Amidase-3 From Thermus Parvatiensis also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Amip Amidase-3 From Thermus Parvatiensis
(pdb code 7b3n). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the
Amip Amidase-3 From Thermus Parvatiensis, PDB code: 7b3n:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 7b3n
Go back to
Sodium Binding Sites List in 7b3n
Sodium binding site 1 out
of 2 in the Amip Amidase-3 From Thermus Parvatiensis
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Amip Amidase-3 From Thermus Parvatiensis within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na205
b:35.5
occ:1.00
|
H
|
A:SER67
|
2.1
|
29.6
|
1.0
|
H
|
B:GLY103
|
2.1
|
27.7
|
1.0
|
O
|
B:HOH352
|
2.7
|
29.1
|
1.0
|
OE1
|
B:GLU106
|
2.8
|
29.1
|
1.0
|
HA
|
B:PRO102
|
2.8
|
29.7
|
1.0
|
N
|
A:SER67
|
3.0
|
29.0
|
1.0
|
N
|
B:GLY103
|
3.0
|
26.2
|
1.0
|
HB3
|
A:PRO65
|
3.0
|
29.4
|
1.0
|
HB2
|
A:LEU66
|
3.1
|
27.6
|
1.0
|
H
|
A:LEU66
|
3.1
|
29.0
|
1.0
|
HB3
|
A:SER67
|
3.2
|
32.7
|
1.0
|
N
|
A:LEU66
|
3.3
|
29.2
|
1.0
|
OG
|
A:SER67
|
3.4
|
37.0
|
1.0
|
OE2
|
B:GLU106
|
3.5
|
30.6
|
1.0
|
CD
|
B:GLU106
|
3.5
|
29.5
|
1.0
|
HG
|
A:SER67
|
3.6
|
37.1
|
0.0
|
CA
|
B:PRO102
|
3.6
|
28.6
|
1.0
|
CB
|
A:SER67
|
3.6
|
32.4
|
1.0
|
HB2
|
A:PRO65
|
3.7
|
29.4
|
1.0
|
H
|
B:GLU105
|
3.7
|
26.5
|
1.0
|
CB
|
A:PRO65
|
3.7
|
28.7
|
1.0
|
HB3
|
B:GLU105
|
3.7
|
28.7
|
1.0
|
C
|
A:PRO65
|
3.8
|
28.3
|
1.0
|
CA
|
A:LEU66
|
3.8
|
29.1
|
1.0
|
C
|
B:PRO102
|
3.8
|
30.6
|
1.0
|
C
|
A:LEU66
|
3.8
|
31.2
|
1.0
|
HA2
|
B:GLY103
|
3.8
|
27.1
|
1.0
|
CB
|
A:LEU66
|
3.8
|
26.8
|
1.0
|
CA
|
A:SER67
|
3.9
|
29.3
|
1.0
|
H
|
B:SER104
|
3.9
|
26.3
|
1.0
|
CA
|
B:GLY103
|
3.9
|
28.2
|
1.0
|
HA
|
A:PRO65
|
4.0
|
28.8
|
1.0
|
CA
|
A:PRO65
|
4.0
|
29.0
|
1.0
|
O
|
B:HOH359
|
4.0
|
40.5
|
1.0
|
O
|
B:HIS101
|
4.1
|
29.1
|
1.0
|
H
|
B:GLU106
|
4.1
|
26.1
|
1.0
|
H
|
A:GLU68
|
4.2
|
28.6
|
1.0
|
N
|
B:SER104
|
4.3
|
25.4
|
1.0
|
C
|
B:GLY103
|
4.4
|
25.6
|
1.0
|
HG
|
A:LEU66
|
4.4
|
28.2
|
1.0
|
HB3
|
B:PRO102
|
4.5
|
31.6
|
1.0
|
HB2
|
B:GLU105
|
4.5
|
28.7
|
1.0
|
N
|
B:GLU105
|
4.5
|
25.3
|
1.0
|
HB3
|
A:LEU66
|
4.5
|
27.6
|
1.0
|
CB
|
B:GLU105
|
4.5
|
29.0
|
1.0
|
HA
|
A:SER67
|
4.5
|
29.8
|
1.0
|
N
|
B:PRO102
|
4.5
|
29.2
|
1.0
|
O
|
A:PRO65
|
4.6
|
30.2
|
1.0
|
HH2
|
B:TRP175
|
4.6
|
37.8
|
1.0
|
HB2
|
A:SER67
|
4.6
|
32.6
|
1.0
|
CB
|
B:PRO102
|
4.7
|
32.1
|
1.0
|
CG
|
A:LEU66
|
4.7
|
28.0
|
1.0
|
C
|
B:HIS101
|
4.7
|
29.9
|
1.0
|
HA
|
A:LEU66
|
4.7
|
29.1
|
1.0
|
HD11
|
A:LEU66
|
4.8
|
27.9
|
1.0
|
HA3
|
B:GLY103
|
4.8
|
27.1
|
1.0
|
N
|
A:GLU68
|
4.9
|
27.0
|
1.0
|
HZ2
|
B:TRP175
|
4.9
|
38.0
|
1.0
|
N
|
B:GLU106
|
4.9
|
24.8
|
1.0
|
C
|
A:SER67
|
4.9
|
29.2
|
1.0
|
CG
|
B:GLU106
|
5.0
|
31.9
|
1.0
|
O
|
B:PRO102
|
5.0
|
30.9
|
1.0
|
|
Sodium binding site 2 out
of 2 in 7b3n
Go back to
Sodium Binding Sites List in 7b3n
Sodium binding site 2 out
of 2 in the Amip Amidase-3 From Thermus Parvatiensis
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Amip Amidase-3 From Thermus Parvatiensis within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Na204
b:50.6
occ:1.00
|
OD2
|
B:ASP136
|
2.4
|
45.4
|
1.0
|
OH
|
C:TYR98
|
2.5
|
33.1
|
1.0
|
HA
|
B:TYR133
|
2.6
|
30.2
|
1.0
|
OE1
|
C:GLU105
|
2.7
|
36.9
|
1.0
|
HE2
|
C:TYR98
|
2.7
|
31.9
|
1.0
|
O
|
B:HOH336
|
2.7
|
40.7
|
1.0
|
HH
|
C:TYR98
|
3.0
|
33.0
|
0.0
|
O
|
B:HOH321
|
3.2
|
55.7
|
1.0
|
CG
|
B:ASP136
|
3.2
|
40.1
|
1.0
|
CZ
|
C:TYR98
|
3.3
|
32.1
|
1.0
|
CE2
|
C:TYR98
|
3.3
|
32.8
|
1.0
|
CD
|
C:GLU105
|
3.3
|
34.0
|
1.0
|
OD1
|
B:ASP136
|
3.5
|
41.8
|
1.0
|
O
|
C:HOH305
|
3.6
|
37.5
|
1.0
|
CA
|
B:TYR133
|
3.6
|
30.4
|
1.0
|
OE2
|
C:GLU105
|
3.6
|
41.0
|
1.0
|
O
|
B:HOH329
|
3.8
|
42.3
|
1.0
|
HB3
|
C:PRO123
|
3.8
|
31.0
|
1.0
|
O
|
C:HOH339
|
3.9
|
43.4
|
1.0
|
HB2
|
B:TYR133
|
4.0
|
31.5
|
1.0
|
HB3
|
B:TYR133
|
4.1
|
31.5
|
1.0
|
O
|
B:TYR133
|
4.1
|
31.6
|
1.0
|
CB
|
B:TYR133
|
4.2
|
31.5
|
1.0
|
HB2
|
B:ASP136
|
4.2
|
34.8
|
1.0
|
O
|
B:LEU132
|
4.2
|
27.7
|
1.0
|
N
|
B:TYR133
|
4.3
|
28.9
|
1.0
|
HD3
|
C:PRO123
|
4.3
|
31.1
|
1.0
|
C
|
B:TYR133
|
4.3
|
29.4
|
1.0
|
CB
|
B:ASP136
|
4.4
|
34.0
|
1.0
|
HG3
|
C:PRO123
|
4.4
|
31.2
|
1.0
|
HB2
|
C:GLU105
|
4.4
|
29.9
|
1.0
|
CG
|
C:GLU105
|
4.5
|
33.3
|
1.0
|
H
|
B:ASP136
|
4.5
|
31.8
|
1.0
|
C
|
B:LEU132
|
4.5
|
31.8
|
1.0
|
HG2
|
B:ARG131
|
4.5
|
37.1
|
1.0
|
HG3
|
C:GLU105
|
4.6
|
32.4
|
1.0
|
CE1
|
C:TYR98
|
4.6
|
29.7
|
1.0
|
CD2
|
C:TYR98
|
4.6
|
30.2
|
1.0
|
HG3
|
B:ARG131
|
4.7
|
37.0
|
1.0
|
CB
|
C:PRO123
|
4.7
|
30.7
|
1.0
|
HB2
|
B:ASP135
|
4.8
|
33.2
|
1.0
|
HE
|
B:ARG131
|
4.9
|
38.6
|
1.0
|
CG
|
C:PRO123
|
4.9
|
31.7
|
1.0
|
H
|
B:TYR133
|
4.9
|
30.0
|
1.0
|
CB
|
C:GLU105
|
5.0
|
29.1
|
1.0
|
HE1
|
C:TYR98
|
5.0
|
30.1
|
1.0
|
HD2
|
C:TYR98
|
5.0
|
30.9
|
1.0
|
HB3
|
B:ASP136
|
5.0
|
34.8
|
1.0
|
|
Reference:
S.Freitag-Pohl,
E.Pohl.
Amip Amidase-3 From Thermus Parvatiensis To Be Published.
Page generated: Tue Oct 8 16:05:32 2024
|